Atomistry » Bromine » PDB 5mrm-5o0j » 5n2a
Atomistry »
  Bromine »
    PDB 5mrm-5o0j »
      5n2a »

Bromine in PDB 5n2a: Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form

Enzymatic activity of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form

All present enzymatic activity of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form:
2.8.4.1;

Protein crystallography data

The structure of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form, PDB code: 5n2a was solved by T.Wagner, C.E.Wegner, U.Ermler, S.Shima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.85 / 2.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 127.699, 127.699, 160.376, 90.00, 90.00, 120.00
R / Rfree (%) 19.8 / 22.1

Other elements in 5n2a:

The structure of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form also contains other interesting chemical elements:

Nickel (Ni) 1 atom
Potassium (K) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form (pdb code 5n2a). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form, PDB code: 5n2a:

Bromine binding site 1 out of 1 in 5n2a

Go back to Bromine Binding Sites List in 5n2a
Bromine binding site 1 out of 1 in the Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Trigonal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Br301

b:94.2
occ:1.00
 NZ C:LYS13 3.3 86.5 1.0
NH1 C:ARG215 3.4 51.9 1.0
CB C:ARG215 3.7 61.0 1.0
CA C:GLY225 3.8 57.1 1.0
CD C:ARG215 4.0 66.8 1.0
CE C:LYS13 4.1 79.6 1.0
C C:GLY225 4.2 59.7 1.0
CG C:ARG215 4.2 64.3 1.0
O C:ARG215 4.4 66.3 1.0
CZ C:ARG215 4.5 70.6 1.0
O C:GLY225 4.5 60.2 1.0
CG2 C:VAL226 4.6 57.2 1.0
N C:VAL226 4.7 54.5 1.0
CA C:ARG215 4.7 63.0 1.0
NE C:ARG215 4.7 65.6 1.0
C C:ARG215 4.8 67.2 1.0
O C:ASP224 4.9 63.9 1.0

Reference:

T.Wagner, C.E.Wegner, J.Kahnt, U.Ermler, S.Shima. Phylogenetic and Structural Comparisons of the Three Types of Methyl Coenzyme M Reductase From Methanococcales and Methanobacteriales. J.Bacteriol. V. 199 2017.
ISSN: ESSN 1098-5530
PubMed: 28559298
DOI: 10.1128/JB.00197-17
Page generated: Thu Jul 11 00:24:53 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy